Evidence for a signal peptide at the amino‐terminal end of human mitochondrial aldehyde dehydrogenase

@article{Braun1987EvidenceFA,
  title={Evidence for a signal peptide at the amino‐terminal end of human mitochondrial aldehyde dehydrogenase},
  author={Thomas Braun and Eva Bober and Surjit Singh and Dharam P. Agarwal and Heinz Werner Goedde},
  journal={FEBS Letters},
  year={1987},
  volume={215}
}

Sequence of the signal peptide for rat liver mitochondrial aldehyde dehydrogenase.

Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences.

Comparisons with the amino acid sequences of other aldehyde dehydrogenases support the suggestion that the NAD-binding domain may be located in the middle portion of the mature enzyme.

Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase.

The expressed mitochondrial iso enzyme could be recognized by antibodies raised against rat mitochondrial ALDH, whereas the cytosolic isozyme could be recognizing by antibody raised against horse cytOSolic ALDH.

Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde.

Human liver aldehyde dehydrogenase (E3 isozyme), with wide substrate specificity and low Km for 4-aminobutyraldehyde, was only recently characterized [Kurys, G., Ambroziak, W. & Pietruszko, R. (1989)

Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme.

Unexpectedly, positions with residues unique to one of the four enzymes are about twice as common in both of the horse proteins than in either of the human proteins, showing that not only functional properties of the protein, but also other factors, such as generation time, are important for enzyme divergence.

Structural organization of aldehyde dehydrogenases probed by limited proteolysis.

The internally cleaved subunits retain a tetrameric configuration as calculated from exclusion chromatography and polyacrylamide gel electrophoresis under native conditions, suggesting that the quaternary structure is not dependent on covalently linked domains within the subunits.

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A cytosolic protein contains a cryptic mitochondrial targeting signal

Cytosolic dihydrofolate reductase from mouse contains a cryptic mitochondrial targeting sequence. If this sequence is attached to the amino terminus of 'passenger' proteins which by themselves cannot

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A non‐mitochondrial protein can be transported into the mitochondrial matrix if it is fitted with a mitochondrial targeting sequence.

Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme.

Analysis of CNBr fragments and other peptides from human liver cytoplasmic aldehyde dehydrogenase enabled determination of the complete primary structure of this protein, supporting the concept that the enzyme is a homotetramer.

Chromosomal assignment of the genes for human aldehyde dehydrogenase-1 and aldehyde dehydrogenase-2.

Chromosomal assignment of the genes for two major human aldehyde dehydrogenase isozymes, ALDH1 and ALDH2, were determined and AL DH1 was assigned to the long arm of human chromosome 9 andALDH2 to chromosome 12.

Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2.

The degree of homology between human ALDH1 and ALDH2 is 66% for the coding regions of their cDNAs and 69% at the protein level and no significant homology was found in their 3' untranslated regions.

Import and processing of hybrid proteins by mammalian mitochondria in vitro.

Normal and hybrid proteins were synthesized following transcription of pSP64 recombinant plasmids with SP6 polymerase and translation of resultant mRNAs in a rabbit reticulocyte lysate. The precursor

Isolation of repetitive clones from human muscle cDNA library

Human fetal muscle cDNA library was screened with aβ-myosin heavy chain gene fragment containing Alu sequences and two cDNA clones AI and BII with 1.8 and 3 kb inserts respectively, which appeared to contain repetitive sequences as well as single copy regions.

The role of alcohol dehydrogenase and aldehyde dehydrogenase isozymes in alcohol metabolism, alcohol sensitivity, and alcoholism.

It is demonstrated that the isozymes of ALDH may play an important role in the pathogenesis of alcohol-related organ damage and in the biological sensitivity to alcohol in certain ethnic groups.

Functional messenger RNAs are produced by SP6 in vitro transcription of cloned cDNAs.

The method of mRNA synthesis involves in vitro transcription of cDNAs which have been cloned into SP6 vectors and enables one to produce large amounts of mRNA and consequently protein from any cDNA clone.